Ubiquitination is essential for recovery of cellular activities after heat shock

<jats:title>Tailoring stress responses</jats:title> <jats:p> When faced with environmental stress, cells respond by shutting down cellular processes such as translation and nucleocytoplasmic transport. At the same time, cells preserve cytoplasmic messenger RNAs in structures known as stress granules, and many cellular proteins are modified by the covalent addition of ubiquitin, which has long been presumed to reflect degradation of stress-damaged proteins (see the Perspective by Dormann). Maxwell <jats:italic>et al.</jats:italic> show that cells generate distinct patterns of ubiquitination in response to different stressors. Rather than reflecting the degradation of stress-damaged proteins, this ubiquitination primes cells to dismantle stress granules and reinitiate normal cellular activities once the stress is removed. Gwon <jats:italic>et al.</jats:italic> show that persistent stress granules are degraded by autophagy, whereas short-lived granules undergo a process of disassembly that is autophagy independent. The mechanism of this disassembly depends on the initiating stress. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , abc3593 and abf6548, this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" related-article-type="in-this-issue" xlink:href="10.1126/science.abc3593">eabc3593</jats:related-article> and p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" related-article-type="in-this-issue" xlink:href="10.1126/science.abf6548">eabf6548</jats:related-article> ; see also abj2400, p. <jats:related-article issue="6549" page="1393" related-article-type="in-this-issue" vol="372">1393</jats:related-article> </jats:p>